| http://purl.uniprot.org/citations/12359732 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12359732 | http://www.w3.org/2000/01/rdf-schema#comment | "Substrate binding to the phosphodiesterase-5 (PDE5) catalytic site increases cGMP binding to the regulatory domain (R domain). The latter promotes PDE5 phosphorylation by cyclic nucleotide-dependent protein kinases, which activates catalysis, enhances allosteric cGMP binding, and causes PDE5A1 to apparently elongate. A human PDE5A1 R domain fragment (Val(46)-Glu(539)) containing the phosphorylation site (Ser(102)) and allosteric cGMP-binding sites was studied. The rate, cGMP dependence, and stoichiometry of phosphorylation of the PDE5 R domain by the catalytic subunit of cAMP-dependent protein kinase are comparable with that of the holoenzyme. Migration in native polyacrylamide gels suggests that either cGMP binding or phosphorylation produces distinct conformers of the R domain. Phosphorylation of the R domain increases affinity for cGMP approximately 10-fold (K(D) values 97.8 +/- 17 and 10.0 +/-0.5 nm for unphospho- and phospho-R domains, respectively). [(3)H]cGMP dissociates from the phospho-R domain with a single rate (t(12) = 339 +/-30 min) compared with the biphasic pattern of the unphospho-R domain (t(12) = 39.0 +/- 4.8 and 265 +/-28 min, for the fast and slow components, respectively). Thus, cGMP-directed regulation of PDE5 phosphorylation and the resulting increase in cGMP binding affinity occur largely within the R domain. Conformational change(s) elicited by phosphorylation of the R domain within the PDE5 holoenzyme may also cause or participate in stimulating catalysis."xsd:string |
| http://purl.uniprot.org/citations/12359732 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m206088200"xsd:string |
| http://purl.uniprot.org/citations/12359732 | http://purl.uniprot.org/core/author | "Liu L."xsd:string |
| http://purl.uniprot.org/citations/12359732 | http://purl.uniprot.org/core/author | "Kotera J."xsd:string |
| http://purl.uniprot.org/citations/12359732 | http://purl.uniprot.org/core/author | "Francis S.H."xsd:string |
| http://purl.uniprot.org/citations/12359732 | http://purl.uniprot.org/core/author | "Corbin J.D."xsd:string |
| http://purl.uniprot.org/citations/12359732 | http://purl.uniprot.org/core/author | "Thompson W.J."xsd:string |
| http://purl.uniprot.org/citations/12359732 | http://purl.uniprot.org/core/author | "Bessay E.P."xsd:string |
| http://purl.uniprot.org/citations/12359732 | http://purl.uniprot.org/core/author | "Grimes K.A."xsd:string |
| http://purl.uniprot.org/citations/12359732 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12359732 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/12359732 | http://purl.uniprot.org/core/pages | "47581-47587"xsd:string |
| http://purl.uniprot.org/citations/12359732 | http://purl.uniprot.org/core/title | "Phosphorylation of isolated human phosphodiesterase-5 regulatory domain induces an apparent conformational change and increases cGMP binding affinity."xsd:string |
| http://purl.uniprot.org/citations/12359732 | http://purl.uniprot.org/core/volume | "277"xsd:string |
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